Introduction
Gelatin is an important hydrocolloid which has
widespread used in food applications. In generally,
mammalian gelatin has been utilized due to its
high melting, gelling point and thermo-reversibility
(Gudmundsson, 2002). It is a high molecular weight
and water-soluble protein. All the amino acids
are present in gelatin except tryptophan and have
low in methionine, cystine and tyrosine due to the
degradation during hydrolysis (Jamilah and Harvinder
2002; Chapman and Hall, 1997). The amino acid
compositon and sequence in gelatin are different
from one source to another but always consists of
large amounts of glycine, proline and hydroxyproline
(Gilsenan, and Ross-Murphy, 2000). It is repeated
with typical sequence, Gly-X-Y where glycine is the
most abundant amino acid in gelatin; X and Y are
mostly proline and hydroxyproline, respectively. 25%
of dry gelatin contains proline and hydroxyproline
that stabilize its structure (Russell et al., 2007).
The chemical properties of gelatin are affected
by amino acid composition, which is similar to that
of the parent collagen, thus influence by animals
species and type of tissues. The differences in
molecular weight distribution were also affected its
chemical properties which result from the variation
in the nature or extraction conditions (Zhou and
Regenstein, 2006). Bovine and porcine skin gelatins
are widely utilized in food manufacturing because
the sources are more available. Gelatin from bovine
skin produced from alkaline treatment is known as
type B gelatin while porcine skin gelatin produced
from acidic treatment is known as type A gelatin.
They may possess different characteristics which
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Determination of turbidity
The turbidity of PSG and BSG solution (6.67%
w/v) at different pH (3-10) was determined according
to preferred method (Aewsiri et al., 2008). The
samples were dissolved in distilled water at 60oC
and the pH of solution was adjusted with either 6
N NaOH or HCl. The turbidity was determined by
measuring the absorbance at 360 nm using U-2810
Polypeptides pattern
The polypeptide patterns of BSG and PSG are
shown in Figure 1. The polypeptides bands were
similar for both gelatins. The findings were in
agreement with Gudmundson, 2002. The distinct
bands with molecular weight approximately of
220 and 100 kDa could be represent and chain,
respectively. The polypeptides with molecular weight
below than 100 kDa in BSG and PSG did not obtain
as expected, meaning that the studied gelatins had
high molecular weight protein.
Table 1. Amino acid composition of bovine and porcine
skin gelatin
Amino acid
Nonpolar
hydrophobic
Alanine
Valine
Leucine
Isoleucine
Phenylalanine
Methionine
Proline
Total
Polar uncharged
Glycine
Serine
Threonine
Tyrosine
Total
33
10
12
7
10
4
63
139
80
26
29
12
27
10
151
335
108
15
10
2
135
239
35
26
7
307
17
34
51
41
83
124
11
47
Not detected
58
27
111
Not detected
138
Polar acidic
Aspartic acid
Glutamic acid
Total
Polar basic
Lysine
Arginine
Histidine
Total
BSG: bovine skin gelatin; PSG: porcine skin gelatin; samples were run duplicates; each
involves 2 batches of gelatins.
M
220 kDa
100 kDa
BSG
PSG
60 kDa
45 kDa
815
Force (g)
BSG
193.49 2.09a
234.00 0.46bc
251.03 2.92c
251.40 1.62
266.69 6.67dd
267.63 5.80d
270.35 8.02c
247.09 1.80
PSG
330.57 0.81be
372.95 0.45 a
326.47 0.07d
357.87 1.95c
350.42 1.05 f
389.04 0.29
415.10 1.21gc
348.57 2.36
Different letters within same column denote significant differences (P < 0.05). BSG: bovine
skin gelatin; PSG: porcine skin gelatine. Mean SD from duplicate determinations.
30 kDa
20 kDa
Figure 1. Polypeptide patterns of bovine and porcine skin gelatin.
M: protein marker, BSG: bovine skin gelatin; PSG: porcine skin
gelatin; and chains: protein component of gelatin.
Effect of pH on turbidity
The turbidity of BSG and PSG was influenced by
pH as shown in Table 3. BSG had higher turbidity
than that of PSG at all pHs. The turbidity of BSG
was highest at pH 7 and decreased at alkaline pHs.
PSG showed the highest turbidity at pH 9 although
its absorbance was slightly lower at pH 6 and 7.
The maximum turbidity of gelatins occurred at
their isoelectric point (Poppe, 1997). For PSG, its
isoelectric point might be at pH 9, as it showed a
maximum turbidity while for BSG, pH 7 might not
be its pI because BSG was type B alkaline-processed
gelatin. This type of gelatins has isoelectric point
ranged between pH 4.8-5.0 as reported (Aewsiri et al.,
2008). At pH close to isoelectric point, aggregation of
protein molecules occurs and reduces its interaction
with water molecules (Vojdani, 1996).
816
PSG
0.055 0.001a
0.065 0.000be
0.078 0.001
0.069 0.001dc
0.073 0.001 f
0.083 0.001
0.087 0.001g
Different letters within same column denote significant differences (P < 0.05). BSG: bovine
skin gelatin; PSG: porcine skin gelatin. Mean SD from duplicate determinations.
FE (%)
FS (%)
0 min
30 min
BSG (2%)
93.00 2.65b
91.67 3.21b
(3%)
94.67 1.53
93.67 1.53b
(4%)
91.00 1.00b
89.33 1.53b
(5%)
72.33 5.51
86.50 5.51a
PSG (2%)
90.00 1.00c
87.67 2.08c
(3%)
(4%)
93.00 1.00c
70.00 10.44b
88.67 2.52c
68.33 9.29b
(5%)
53.00 1.00a
51.33 0.58a
Different letters in the same column within the same gelatin denote significant differences
(P<0.05). FE: foam expansion; FS: foam stability. Mean SD from duplicate determinations.
817